Controlling Polymer Assembly with Precise Design

While the development of synthetic techniques to produce sequence-controlled polymers holds the promise of making polymers with the complexity and functionality of proteins, the design strategies for engineering these kinds of hierarchical architectures are not yet sufficiently sophisticated. We combine experimental and molecular dynamics simulation techniques to understand how the monomer sequence of polypeptoids impacts polymer chain shape and assembly. To explore these effects, we have studied the conformation of polypeptoid chains in solution via neutron scattering and double electron-electron resonance spectroscopy to understand how the number and location of hydrophobic and chiral monomers leads to changes in radius of gyration and end-to-end distance. We also use structural control enabled by sequence-defined polypeptoids to demonstrate that water behavior can be tuned near polymeric surfaces. This system simultaneously offers both a route to control polymer chain shape and functional group position as well as an unique opportunity to map water diffusivity at different locations within the assembly.